2nul Summary



The structure was published by Edwards, K.J., Ollis, D.L., and Dixon, N.E., in 1997 in a paper entitled "Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1996.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PEPTIDYLPROLYL ISOMERASE. This molecule has the UniProt identifier P23869 (PPIB_ECOLI)search. The sample contained 164 residues which is 100% of the natural sequence. Out of 164 residues 157 were observed and are deposited in the PDB.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PEPTIDYLPROLYL ISOMERASE P23869 (1-164) (PPIB_ECOLI)search Escherichia coli K-12search 100% 164 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P23869 (1 - 164) PEPTIDYLPROLYL ISOMERASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P23869) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P23869) protein peptidyl-prolyl isomerizationsearch protein foldingsearch peptidyl-prolyl cis-trans isomerase activitysearch protein bindingsearch isomerase activitysearch cytoplasmsearch cytosolsearch

Chain InterPro annotation
A Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainsearch Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved sitesearch Cyclophilin-like domainsearch